Proteomics

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Total proteome analysis of WT vs TRAP1 KO in HCT-116 and HEK-293T cells grown on different carbon sources.

ABSTRACT: The molecular chaperone TRAP1, the mitochondrial isoform of cytosolic HSP90, remains poorly understood with respect to its pivotal role in the regulation of mitochondrial metabolism. To characterize the impact of TRAP1 in maintaining the cellular proteome under different energy sources we carried out a label free quantitation (LFQ) MS analysis of the total cellular proteome with WT and KO HEK293T and HCT116 cells cultured with the three different cocktails of carbon sources (Glc + Pyr + Gln, Gal + Pyr only, Gln only). Linked manuscript : Abhinav Joshi, Li Dai, Yanxin Liu, Jungsoon Lee, Nastaran Mohammadi Ghahhari, Gregory Segala, Kristin Beebe, Francis T.F. Tsai, David A. Agard, Len Neckers, and Didier Picard* (*corresponding author).

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Manfredo Quadroni  

LAB HEAD: Didier Picard

PROVIDER: PXD015828 | Pride | 2020-01-16

REPOSITORIES: Pride

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The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis.

Joshi Abhinav A   Dai Li L   Liu Yanxin Y   Lee Jungsoon J   Ghahhari Nastaran Mohammadi NM   Segala Gregory G   Beebe Kristin K   Jenkins Lisa M LM   Lyons Gaelyn C GC   Bernasconi Lilia L   Tsai Francis T F FTF   Agard David A DA   Neckers Len L   Picard Didier D  

BMC biology 20200127 1

<h4>Background</h4>The molecular chaperone TRAP1, the mitochondrial isoform of cytosolic HSP90, remains poorly understood with respect to its pivotal role in the regulation of mitochondrial metabolism. Most studies have found it to be an inhibitor of mitochondrial oxidative phosphorylation (OXPHOS) and an inducer of the Warburg phenotype of cancer cells. However, others have reported the opposite, and there is no consensus on the relevant TRAP1 interactors. This calls for a more comprehensive an  ...[more]

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